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Protein

Beta-1,3-N-acetylglucosaminyltransferase radical fringe

Gene

Rfng

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Inhibits Notch signaling in postmitotic neurons of the brain. It may play a role in adult brain and in neurogenesis. It may play a role in limb development (By similarity).By similarity

Catalytic activityi

Transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor.

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei77SubstrateBy similarity1
Binding sitei150SubstrateBy similarity1
Metal bindingi151ManganeseBy similarity1
Active sitei240By similarity1
Metal bindingi264ManganeseBy similarity1

GO - Molecular functioni

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • negative regulation of Notch signaling pathway Source: RGD
  • nervous system development Source: UniProtKB-KW
  • pattern specification process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Keywords - Biological processi

Differentiation, Neurogenesis

Keywords - Ligandi

Manganese, Metal-binding

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,3-N-acetylglucosaminyltransferase radical fringe (EC:2.4.1.222)
Alternative name(s):
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
Gene namesi
Name:Rfng
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621322. Rfng.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6CytoplasmicSequence analysis6
Transmembranei7 – 29Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini30 – 334LumenalSequence analysisAdd BLAST305

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002191871 – 334Beta-1,3-N-acetylglucosaminyltransferase radical fringeAdd BLAST334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi116N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi117 ↔ 128By similarity
Disulfide bondi146 ↔ 210By similarity
Disulfide bondi314 ↔ 323By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9R1U9.
PRIDEiQ9R1U9.

Expressioni

Tissue specificityi

Most abundantly expressed in adult brain. Expressed in most neurons of the brain but not in glial cells. Also detected to a lower extent in adult lung and kidney.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067562.

Structurei

3D structure databases

ProteinModelPortaliQ9R1U9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II9W. Eukaryota.
ENOG410XS8Y. LUCA.
HOVERGENiHBG007986.
InParanoidiQ9R1U9.
KOiK05948.
PhylomeDBiQ9R1U9.

Family and domain databases

InterProiIPR017374. Fringe.
IPR003378. Fringe-like.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFiPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9R1U9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRVRRVLCR ACLALAAVLA VLLLLPLPLP LPLPLPRAPA PDPGRVPTGS
60 70 80 90 100
LTLEVSRLQP DDVFIAVKTT RKNHGPRLRL LLRTWISRAP RQTFIFTDGD
110 120 130 140 150
DPELQLLAGS QMINTNCSAV RTRQALCCKM SVEYDKFIES GRKWFCHVDD
160 170 180 190 200
DNYVNPKSLL HLLSTFSSNQ DIYLGRPSLD HPIEATERVQ GGGTSNTVKF
210 220 230 240 250
WFATGGAGFC LSRGLALKMS PWASLGSFMS TAERVRLPDD CTVGYIVEGL
260 270 280 290 300
LGARLLHSPL FHSHLENLQK LPSGAVLQQV TLSYGGPENP HNVVNVAGSF
310 320 330
SIRQDPTRFQ SVHCLLYPDT HWCPMKNRGK EAFQ
Length:334
Mass (Da):36,993
Last modified:May 1, 2000 - v1
Checksum:iED0D21CFD5BFB40A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016486 mRNA. Translation: BAA82742.1.
RefSeqiNP_068621.1. NM_021849.1.
UniGeneiRn.168817.

Genome annotation databases

GeneIDi60433.
KEGGirno:60433.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016486 mRNA. Translation: BAA82742.1.
RefSeqiNP_068621.1. NM_021849.1.
UniGeneiRn.168817.

3D structure databases

ProteinModelPortaliQ9R1U9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067562.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Proteomic databases

PaxDbiQ9R1U9.
PRIDEiQ9R1U9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi60433.
KEGGirno:60433.

Organism-specific databases

CTDi5986.
RGDi621322. Rfng.

Phylogenomic databases

eggNOGiENOG410II9W. Eukaryota.
ENOG410XS8Y. LUCA.
HOVERGENiHBG007986.
InParanoidiQ9R1U9.
KOiK05948.
PhylomeDBiQ9R1U9.

Miscellaneous databases

PROiQ9R1U9.

Family and domain databases

InterProiIPR017374. Fringe.
IPR003378. Fringe-like.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFiPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRFNG_RAT
AccessioniPrimary (citable) accession number: Q9R1U9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: May 1, 2000
Last modified: October 5, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.